1CQD

THE 2.1 ANGSTROM STRUCTURE OF A CYSTEINE PROTEASE WITH PROLINE SPECIFICITY FROM GINGER RHIZOME, ZINGIBER OFFICINALE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	93
Detector technology	IMAGE PLATE
Collection date	1997-08-15
Detector	RIGAKU RAXIS II
Spacegroup name	P 1 21 1
Unit cell lengths	93.980, 45.450, 110.040
Unit cell angles	90.00, 105.03, 90.00

Refinement procedure

Resolution	25.000 - 2.100
R-factor	0.214 *
Rwork	0.213
R-free	0.24800 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	24.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.191 *
Number of reflections	58449
<I/σ(I)>	8	3.8
Completeness [%]	99.7	94.9 *
Redundancy	5	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.2	18 *	0.1 M SODIUM ACETATE BUFFER (PH 5.2) CONTAINING 0.1 M AMMONIUM SULFATE, 26% POLYETHYLENE GLYCOL MONOMETHYLETHER 2000, AND 2.5 MM SODIUM TETRATHIONATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	mPEG2000	26 (%)
3	1	reservoir	ammonium sulfate	0.2 (M)
4	1	reservoir	sodium acetate	0.1 (M)